hemL

Functionⁱ

Catalytic activityⁱ

(S)-4-amino-5-oxopentanoate = 5-aminolevulinate.UniRule annotation

Cofactorⁱ

pyridoxal 5'-phosphateUniRule annotation

Pathwayⁱ: protoporphyrin-IX biosynthesis

This protein is involved in step 2 of the subpathway that synthesizes 5-aminolevulinate from L-glutamyl-tRNA(Glu).UniRule annotation
Proteins known to be involved in the 2 steps of the subpathway in this organism are:

Glutamyl-tRNA reductase (hemA)
Glutamate-1-semialdehyde 2,1-aminomutase (hemL)

This subpathway is part of the pathway protoporphyrin-IX biosynthesis, which is itself part of Porphyrin-containing compound metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes 5-aminolevulinate from L-glutamyl-tRNA(Glu), the pathway protoporphyrin-IX biosynthesis and in Porphyrin-containing compound metabolism.

GO - Molecular functionⁱ

glutamate-1-semialdehyde 2,1-aminomutase activity Source: UniProtKB-EC
pyridoxal phosphate binding Source: InterPro
transaminase activity Source: InterPro

Complete GO annotation...

GO - Biological processⁱ

protoporphyrinogen IX biosynthetic process Source: UniProtKB-UniPathway

Complete GO annotation...

Keywordsⁱ

Molecular function	Isomerase
Biological process	Porphyrin biosynthesis
Ligand	Pyridoxal phosphate

Enzyme and pathway databases

UniPathwayⁱ	UPA00251; UER00317.

UniPathwayⁱ

UPA00251; UER00317.

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Glutamate-1-semialdehyde 2,1-aminomutaseUniRule annotation (EC:5.4.3.8UniRule annotation) Short name: GSAUniRule annotation Alternative name(s): Glutamate-1-semialdehyde aminotransferaseUniRule annotation Short name: GSA-ATUniRule annotation
Gene namesⁱ	Name:hemLUniRule annotation Ordered Locus Names:DIP0409
Organismⁱ	Corynebacterium diphtheriae (strain ATCC 700971 / NCTC 13129 / Biotype gravis)
Taxonomic identifierⁱ	257309 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Bacteria › Terrabacteria group › Actinobacteria › Actinobacteria › Corynebacteriales › Corynebacteriaceae › Corynebacterium › Corynebacterium diphtheriae
Proteomesⁱ	UP000002198 Componentⁱ: Chromosome

Subcellular locationⁱ

Cytoplasm
UniRule annotation
Manual assertion according to rulesⁱ
- HAMAP-Rule:MF_00375

GO - Cellular componentⁱ

cytoplasm Source: UniProtKB-SubCell

Complete GO annotation...

Keywords - Cellular componentⁱ

Cytoplasm

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
ChainⁱPRO_0000120404	1 – 430	Glutamate-1-semialdehyde 2,1-aminomutaseAdd BLAST		430

Amino acid modifications

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Modified residueⁱ	267	N6-(pyridoxal phosphate)lysineUniRule annotation		1

Interactionⁱ

Subunit structureⁱ

Homodimer.UniRule annotation

Structureⁱ

3D structure databases

ProteinModelPortalⁱ	Q6NJJ2.
SMRⁱ	Q6NJJ2.
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Family & Domainsⁱ

Sequence similaritiesⁱ

Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. HemL subfamily.UniRule annotation

Phylogenomic databases

HOGENOMⁱ	HOG000020210.
KEGG Orthology (KO) More...KOⁱ	K01845.
OMAⁱ	WGPLIFG.

Family and domain databases

Conserved Domains Database More...CDDⁱ	cd00610. OAT_like. 1 hit.
Gene3Dⁱ	3.40.640.10. 1 hit. 3.90.1150.10. 2 hits.
HAMAPⁱ	MF_00375. HemL_aminotrans_3. 1 hit.
InterProⁱ	View protein in InterPro IPR004639. 4pyrrol_synth_GluAld_NH2Trfase. IPR005814. Aminotrans_3. IPR015424. PyrdxlP-dep_Trfase. IPR015421. PyrdxlP-dep_Trfase_major_sub1. IPR015422. PyrdxlP-dep_Trfase_sub2.
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF00202. Aminotran_3. 1 hit.
SUPFAMⁱ	SSF53383. SSF53383. 1 hit.
TIGRFAMsⁱ	TIGR00713. hemL. 1 hit.
PROSITEⁱ	View protein in PROSITE PS00600. AA_TRANSFER_CLASS_3. 1 hit.

Sequenceⁱ

Sequence statusⁱ: Complete.

Q6NJJ2-1 [UniParc]FASTA Add to basket

« Hide

        10         20         30         40         50
MTSTQRSQEL FARAQQFTPG GVNSPVRAFG SVGGHARFIQ SAKGSKLYDV 
        60         70         80         90        100
DGNEYVDLVC SWGPMLLGNA HPEIVEAVQK AATNGLSFGA PTEAEVKIAE 
       110        120        130        140        150
MIVDRTSVEE VRMVNSGTEA TMSAVRLARG FTGRPKVIKF DGCYHGHVDA 
       160        170        180        190        200
LLASAGSGVA TFALPDSPGV TGASAADTIV VPYNDSEAVR AAFEAHPDQI 
       210        220        230        240        250
ACVIAEAAAG NMGTVAPQDN FNAKLKEVAH EHGALLILDE VMTGFRTSYN 
       260        270        280        290        300
GWYGVDGVAG DLTTFGKVIS GGLPAAAFGG RADIMRYLAP EGPVYQAGTL 
       310        320        330        340        350
SGNPVAMAAG MKSLELATPE VYDMVRANAD RLAGLLHEAL DREGVAHHIQ 
       360        370        380        390        400
RAATMLSVRF AEGEGHNFDD MKAADTFRFP AFFHALLDNG IYASPSVFET 
       410        420        430
WFVSAALTDD DFDKIEKALR PAAQAAGKAK

Length:430

Mass (Da):45,362

Last modified:July 5, 2004 - v1

Checksum:ⁱ6B94BAA04DD5DE16

GO

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	BX248355 Genomic DNA. Translation: CAE48913.1.
NCBI Reference Sequences More...RefSeqⁱ	WP_010934280.1. NC_002935.2.

Genome annotation databases

EnsemblBacteriaⁱ	CAE48913; CAE48913; DIP0409.
GeneIDⁱ	2649362.
KEGGⁱ	cdi:DIP0409.

Similar proteinsⁱ

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:

100%	UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%	UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%	UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	BX248355 Genomic DNA. Translation: CAE48913.1.
NCBI Reference Sequences More...RefSeqⁱ	WP_010934280.1. NC_002935.2.

3D structure databases

ProteinModelPortalⁱ	Q6NJJ2.
SMRⁱ	Q6NJJ2.
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protocols and materials databases

Structural Biology Knowledgebase	Search...

Structural Biology Knowledgebase

Search...

Genome annotation databases

EnsemblBacteriaⁱ	CAE48913; CAE48913; DIP0409.
GeneIDⁱ	2649362.
KEGGⁱ	cdi:DIP0409.

Phylogenomic databases

HOGENOMⁱ	HOG000020210.
KEGG Orthology (KO) More...KOⁱ	K01845.
OMAⁱ	WGPLIFG.

Enzyme and pathway databases

UniPathwayⁱ	UPA00251; UER00317.

UniPathwayⁱ

UPA00251; UER00317.

Family and domain databases

Conserved Domains Database More...CDDⁱ	cd00610. OAT_like. 1 hit.
Gene3Dⁱ	3.40.640.10. 1 hit. 3.90.1150.10. 2 hits.
HAMAPⁱ	MF_00375. HemL_aminotrans_3. 1 hit.
InterProⁱ	View protein in InterPro IPR004639. 4pyrrol_synth_GluAld_NH2Trfase. IPR005814. Aminotrans_3. IPR015424. PyrdxlP-dep_Trfase. IPR015421. PyrdxlP-dep_Trfase_major_sub1. IPR015422. PyrdxlP-dep_Trfase_sub2.
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF00202. Aminotran_3. 1 hit.
SUPFAMⁱ	SSF53383. SSF53383. 1 hit.
TIGRFAMsⁱ	TIGR00713. hemL. 1 hit.
PROSITEⁱ	View protein in PROSITE PS00600. AA_TRANSFER_CLASS_3. 1 hit.
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	GSA_CORDI
Accessionⁱ	Q6NJJ2Primary (citable) accession number: Q6NJJ2
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	March 1, 2005
	Last sequence update:	July 5, 2004
	Last modified:	June 7, 2017
	This is version 90 of the entry and version 1 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Prokaryotic Protein Annotation Program

UniProtKB

UniParc

Help

UniRef

Proteomes

Annotation systems

Supporting data

UniProtKB - Q6NJJ2 (GSA_CORDI)

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Glutamate-1-semialdehyde 2,1-aminomutase

Select a section on the left to see content.

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">‘Function’</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: protoporphyrin-IX biosynthesis

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Biological processi

Enzyme and pathway databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Cellular componenti

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Amino acid modifications

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Phylogenomic databases

Family and domain databases

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including length and molecular weight.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

Sequence databases

Genome annotation databases

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

3D structure databases

Protocols and materials databases

Genome annotation databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Documents

Functionⁱ

Pathwayⁱ: protoporphyrin-IX biosynthesis

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

GO - Cellular componentⁱ

PTM / Processingⁱ

Interactionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Sequenceⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ